Results 341 to 350 of about 151,994 (387)
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Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase
Applied Microbiology and Biotechnology, 1999Naphthalene 1,2-dioxygenase (Nap dox) and biphenyl 2,3-dioxygenase (Bph dox) are related enzymes that have differentiated during evolution as their specificity has changed. Although their component arrangement is similar, the structure of each component has been modified quite extensively.
D, Barriault, M, Sylvestre
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Cysteine dioxygenase: structure and mechanism
Chemical Communications, 2007AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Joseph, CA, Maroney, MJ
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Applied Microbiology and Biotechnology, 2011
This review details recent progresses in the flavonoid biotransformation by bacterial non-heme dioxygenases, biphenyl dioxygenase (BDO), and naphthalene dioxygenase (NDO), which can initially activate biphenyl and naphthalene with insertion of dioxygen in stereospecfic and regiospecific manners.
Jiyoung, Seo +4 more
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This review details recent progresses in the flavonoid biotransformation by bacterial non-heme dioxygenases, biphenyl dioxygenase (BDO), and naphthalene dioxygenase (NDO), which can initially activate biphenyl and naphthalene with insertion of dioxygen in stereospecfic and regiospecific manners.
Jiyoung, Seo +4 more
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Biochemical and biophysical research communications, 2005
Alpha-dioxygenases constitute a family of fatty acid-metabolizing enzymes recently discovered in plants. The present paper gives a brief overview of the literature dealing with these enzymes and additionally reports the new finding of an alpha-dioxygenase in the moss, Physcomitrella patens, and some properties of this enzyme.
Mats, Hamberg +3 more
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Alpha-dioxygenases constitute a family of fatty acid-metabolizing enzymes recently discovered in plants. The present paper gives a brief overview of the literature dealing with these enzymes and additionally reports the new finding of an alpha-dioxygenase in the moss, Physcomitrella patens, and some properties of this enzyme.
Mats, Hamberg +3 more
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2012
Abstract The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the O 2 -dependent oxidation of l-tryptophan to N -formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a ...
Efimov, I +5 more
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Abstract The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the O 2 -dependent oxidation of l-tryptophan to N -formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a ...
Efimov, I +5 more
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Biochemical and Biophysical Research Communications, 2005
Mats Hamberg +3 more
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Mats Hamberg +3 more
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